Reviewed, UniProtKB/Swiss-Prot Q5ZWN7 (ATPA1_LEGPH)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit alpha 1
    EC=3.6.3.14
Alternative name(s):
    F-ATPase subunit alpha 1
    ATP synthase F1 sector subunit alpha 1

Gene names

Name:	atpA1
Ordered Locus Names:	lpg1048

Organism

Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) [Complete proteome] [HAMAP]

Taxonomic identifier

272624 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

Protein attributes

Sequence length	490 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit By similarity. HAMAP MF_01346
Catalytic activity	ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP MF_01346
Subunit structure	F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a1, b2 and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF1 is attached to CF0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains By similarity. HAMAP MF_01346
Subcellular location	Cell inner membrane; Peripheral membrane protein By similarity HAMAP MF_01346.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell inner membrane Cell membrane Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 490	490	ATP synthase subunit alpha 1 HAMAP MF_01346		PRO_0000238272
Sites
	Site	364	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5ZWN7-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: FAA3FCA1BC7D1AD9	FASTA	490	54,851
	10 20 30 40 50 60 MNWSNTPSFL EKQRQRLERY QFQIKVSEQG RVVSVGDGII WIKGLPGAAI DEILISEDEC 70 80 90 100 110 120 CIAMVFHLTE ELVGAVMLVQ TKKLKAGTPI FPLKRVLSIP VGDKLLGRVI DPLGHPLDGG 130 140 150 160 170 180 EIPPHEEQGL LDRLSPPILH RDFVNRPLYT GNKMLDNLIP IGKGQRELLI GDNGLGKSAL 190 200 210 220 230 240 ALDIVMNQKD KKVYCVYVLI GQKRSTVSST IQLLKEANAL DYTTVVVAQA TALPGLLYLA 250 260 270 280 290 300 PFAGCAIAEH WMKKGLDALV IYDDLSAHAN SYRELSLLLR RPPGREAFPA DIFYLHSRLL 310 320 330 340 350 360 ERSTCLSPAL GGGSMTALPI IETKEGEMAT YIPTNLISIT DGQIFFDESL FSSGFLPAID 370 380 390 400 410 420 ITKSVSRVGG KAQHPQIKKE SGRMKLDYLQ FLDLELFTRF GAKLDAKMQK QIQKGRVLRE 430 440 450 460 470 480 ILKQERFSPL PIEFQLAWLI AYNEGFFDEL NLEDIPKMLK KIEEEIKQST LSLGSPREQW 490 KKAIKEWLMA

References

[1]

"The genomic sequence of the accidental pathogen Legionella pneumophila." Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S. , Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A., Russo J.J. Science 305:1966-1968(2004) [PubMed: 15448271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017354 Genomic DNA. Translation: AAU27134.1.
RefSeq	YP_095081.1.
3D structure databases
SMR	Q5ZWN7. Positions 18-488.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5ZWN7.
Genome annotation databases
GeneID	3080316.
GenomeReviews	Gene locus lpg1048 in contig AE017354_GR.
KEGG	lpn:lpg1048.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0056.
HOGENOM	HBG565875.
OMA	HAQTYRE.
Enzyme and pathway databases
BioCyc	LPNE272624:LPG1048-MONOMER.
Family and domain databases
HAMAP	MF_01346. ATP_synth_alpha_bact. [Tree]
InterPro	IPR005294. ATPase_F1-cplx_asu. IPR017458. ATPase_F1-cplx_asu_C. IPR018118. ATPase_F1/A1-cplx_a/bsu_N. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR020003. ATPase_F1/V1/A1_a/bsu_AS. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. [Graphical view]
PANTHER	PTHR15184:SF3. ATPase_F1_a. 1 hit.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR00962. atpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPA1_LEGPH

Accession

Primary (citable) accession number: Q5ZWN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	November 23, 2004
Last modified:	February 9, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)